| First Author | Sikora M | Year | 2019 |
| Journal | Sci Rep | Volume | 9 |
| Issue | 1 | Pages | 2669 |
| PubMed ID | 30804445 | Mgi Jnum | J:275290 |
| Mgi Id | MGI:6304600 | Doi | 10.1038/s41598-019-38784-4 |
| Citation | Sikora M, et al. (2019) Sex affects N-homocysteinylation at lysine residue 212 of albumin in mice. Sci Rep 9(1):2669 |
| abstractText | The modification of protein lysine residues by the thioester homocysteine (Hcy)-thiolactone has been implicated in cardiovascular and neurodegenerative diseases. However, only a handful of proteins carrying Hcy on specific lysine residues have been identified and quantified in humans or animals. In the present work, we developed a liquid chromatography/mass spectrometry targeted assay, based on multiple reaction monitoring, for quantification of N-Hcy-Lys212 (K212Hcy) and N-Hcy-Lys525 (K525Hcy) sites in serum albumin in mice. Using this assay, we found that female (n = 20) and male (n = 13) Cbs(-/-) mice had significantly elevated levels of K212Hcy and K525Hcy modifications in serum albumin relative to their female (n = 19) and male (n = 17) Cbs(+/-) littermates. There was significantly more K212Hcy modification in Cbs(-/-) males than in Cbs(-/-) females (5.78 +/- 4.21 vs. 3.15 +/- 1.38 units, P = 0.023). Higher K212Hcy levels in males than in females were observed also in Cbs(+/-) mice (2.72 +/- 0.81 vs. 1.89 +/- 1.07 units, P = 0.008). In contrast, levels of the K525Hcy albumin modification were similar between males and females, both in Cbs(-/-) and Cbs(+/-) mice. These findings suggest that the sex-specific K212Hcy modification in albumin might have an important biological function in mice that is not affected by the Cbs genotype. |
